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Proteomic Analysis of Polycyclic Aromatic Hydrocarbons (PAHs) Degradation and Detoxification in Sphingobium chungbukense DJ77

  • Lee, Soo Youn (School of Biological Sciences, Chungbuk National University) ;
  • Sekhon, Simranjeet Singh (School of Biological Sciences, Chungbuk National University) ;
  • Ban, Yeon-Hee (School of Biological Sciences, Chungbuk National University) ;
  • Ahn, Ji-Young (School of Biological Sciences, Chungbuk National University) ;
  • Ko, Jung Ho (College of Veterinary Medicine, Western University of Health Sciences) ;
  • Lee, Lyon (College of Veterinary Medicine, Western University of Health Sciences) ;
  • Kim, Sang Yong (Department of Food Science and Biotechnology, Shin Ansan University) ;
  • Kim, Young-Chang (School of Biological Sciences, Chungbuk National University) ;
  • Kim, Yang-Hoon (School of Biological Sciences, Chungbuk National University)
  • Received : 2016.06.03
  • Accepted : 2016.07.21
  • Published : 2016.11.28

Abstract

Polycyclic aromatic hydrocarbons (PAHs) are commonly present xenobiotics in natural and contaminated soils. We studied three (phenanthrene, naphthalene, and biphenyl) xenobiotics, catabolism, and associated proteins in Sphingobium chungbukense DJ77 by two-dimensional gel electrophoresis (2-DE) analysis. Comparative analysis of the growth-dependent 2-DE results revealed that the intensity of 10 protein spots changed identically upon exposure to the three xenobiotics. Among the upregulated proteins, five protein spots, which were putative dehydrogenase, dioxygenase, and hydrolase and involved in the catabolic pathway of xenobiotic degradation, were induced. Identification of these major multifunctional proteins allowed us to map the multiple catabolic pathway for phenanthrene, naphthalene, and biphenyl degradation. A part of the initial diverse catabolism was converged into the catechol degradation branch. Detection of intermediates from 2,3-dihydroxy-biphenyl degradation to pyruvate and acetyl-CoA production by LC/MS analysis showed that ring-cleavage products of PAHs entered the tricarboxylic acid cycle, and were mineralized in S. chungbukense DJ77. These results suggest that S. chungbukense DJ77 completely degrades a broad range of PAHs via a multiple catabolic pathway.

Keywords

References

  1. Ban YH, Ahn JY, Sekhon SS, Cho SJ, Kim YH, Kim YC. 2016. Identification of inducible proteins in the phenanthrene degrader Sphingomonas chungbukensis DJ77 by 2-dimensional electrophoresis and liquid chromatography/tandem mass spectrometry. Genes Genomics 38: 397-405. https://doi.org/10.1007/s13258-015-0374-2
  2. Carbone V, Hara A, El-Kabbani O. 2008. Structural and functional features of dimeric dihydrodiol dehydrogenase. Cell. Mol. Life Sci. 65: 1461-1474.
  3. Delawary M, Ohtsueo Y, Ohta A. 2003. The dual function of biphenyl-degrading ability of Pseudomonas sp. KKS102: energy acquisition and substrate detoxification. Biosci. Biotechnol. Biochem. 67: 1970-1975. https://doi.org/10.1271/bbb.67.1970
  4. Diaz E, Jimenez J, Nogales J. 2013. Aerobic degradation of aromatic compounds. Curr. Opin. Biotechnol. 24: 431-442. https://doi.org/10.1016/j.copbio.2012.10.010
  5. Fuchs G, Boll M, Heider J. 2011. Microbial degradation of aromatic compounds - from one strategy to four. Nat. Rev. Microbiol. 9: 803-816. https://doi.org/10.1038/nrmicro2652
  6. Goodsell DS. 2004. The molecular perspective: polycyclic aromatic hydrocarbons. Stem Cells 22: 873-874 https://doi.org/10.1634/stemcells.22-5-873
  7. Heukeshoven J, Dernick R. 1985. Characterization of a solvent system for separation of water-insoluble poliovirus proteins by reversed-phase high-performance liquid chromatography. J. Chromatogr. 326: 91-101. https://doi.org/10.1016/S0021-9673(01)87434-3
  8. Hwang S, Kim SJ, Kim CK, Kim Y, Kim SJ, Kim YC. 1999. The phnIJ genes encoding acetaldehyde dehydrogenase (acylating) and 4-hydroxy-2-oxovalerate aldolase in Pseudomonas sp. DJ77 and their evolutionary implications. Biochem. Biophys. Res. Commun. 256: 469-473. https://doi.org/10.1006/bbrc.1999.0355
  9. Jimenez JI, Nogales J, Garcia JL, Diaz E. 2010. A genomic view of the catabolism of aromatic compounds in Pseudomonas, pp. 1297-1325. In Timmis KN (ed.). Handbook of Hydrocarbon and Lipid Microbiology. Springer, Berlin-Heidelberg.
  10. Johnson CW, Beckham GT. 2015. Aromatic catabolic pathway selection for optimal production of pyruvate and lactate from lignin. Metab. Eng. 28: 240-247. https://doi.org/10.1016/j.ymben.2015.01.005
  11. Kim S, Kweon OK, Kim Y, Kim CK, Lee KS, Kim YC. 1997. Localization and sequence analysis of the phnH gene encoding 2-hydroxypent-2,4-dienoate hydratase in Pseudomonas sp. strain DJ77. Biochem. Biophys. Res. Commun. 238: 56-60. https://doi.org/10.1006/bbrc.1997.6959
  12. Kim S, Shin HJ, Kim Y, Kim SJ, Kim YC. 1997. Nucleotide sequence of the Pseudomonas sp. DJ77 phnG gene encoding 2-hydroxymuconic semialdehyde dehydrogenase. Biochem. Biophys. Res. Commun. 240: 41-45. https://doi.org/10.1006/bbrc.1997.7595
  13. Kim SJ, Chun J, Bae KS, Kim YC. 2000. Polyphasic assignment of an aromatic degrading Pseudomonas sp., strain DJ77, in the genus Sphingomonas as Sphingomonas chungbukensis sp. nov. Int. J. Syst. Evol. Microbiol. 50: 1641-1647. https://doi.org/10.1099/00207713-50-4-1641
  14. Lee SE, Seo JS, Keun YS, Lee KJ, Li QX. 2007. Fluoranthene metabolism and associated proteins in Mycobacterium sp. JS14. Proteomics 7: 2059-2069. https://doi.org/10.1002/pmic.200600489
  15. Lee SY, Kim YH, Min J. 2010. Conversion of phenol to glutamate and proline in Corynebacterium glutamicum is regulated by transcriptional regulator ArgR. Appl. Microbiol. Biotechnol. 85: 713-720. https://doi.org/10.1007/s00253-009-2206-2
  16. Lyu Y, Zheng W, Zheng T, Tian Y. 2014. Biodegradation of polycyclic aromatic hydrocarbons by Novosphingobium pentaromativorans US6-1. PLoS One 9: e101438. https://doi.org/10.1371/journal.pone.0101438
  17. Majoul T, Bancel E, Triboi E, Hamida JB, Branlard G. 2003. Proteomic analysis of the effect of heat stress on hexaploid wheat grain: characterization of heat-responsive proteins from total endosperm. Proteomics 3: 175-183. https://doi.org/10.1002/pmic.200390026
  18. Nandhagopal N, Senda T, Hatta T, Yamada A, Masai E, Fukuda M, Mitsui Y. 1997. Three-dimensional structure of microbial 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic acid (HpdA) hydrolase (BphD enzyme) from Rhodococcus sp. strain Rha1, in the PCB degradation pathway. Proc. Jpn. Acad. Ser. B 73: 154. https://doi.org/10.2183/pjab.73.154
  19. Pinyakong O, Habe H, Omori T. 2003. The unique aromatic catabolic genes in sphingomonads degradations degrading polycyclic aromatic hydrocarbons (PAHs). J. Gen. Appl. Microbiol. 49: 1-19. https://doi.org/10.2323/jgam.49.1
  20. Ramdine G, Fichet D, Louis M, Lemoine S. 2012. Polycyclic aromatic hydrocarbons (PAHs) in surface sediment and oysters (Crassostrea rhizophorae) from mangrove of Guadeloupe: levels, bioavailability, and effects. Ecotoxicol. Environ. Saf. 79: 80-89. https://doi.org/10.1016/j.ecoenv.2011.12.005
  21. Shin HJ, Kim SJ, Kim YC. 1997. Sequence analysis of the phnD gene encoding 2-hydroxymuconic semialdehyde hydrolase in Pseudomonas sp. strain DJ77. Biochem. Biophys. Res. Commun. 232: 288-291. https://doi.org/10.1006/bbrc.1997.6279
  22. Song MK, Kim YJ, Song M, Choi HS, Ryu JC. 2011. Doseresponse functional gene analysis by exposure to 3 different polycyclic aromatic hydrocarbons in human hepatocytes. Mol. Cell. Toxicol. 7: 221-232. https://doi.org/10.1007/s13273-011-0028-7
  23. Stolz A. 2009. Molecular characteristics of xenobiotic-degrading sphingomonads. Appl. Microbiol. Biotechnol. 81: 793-811. https://doi.org/10.1007/s00253-008-1752-3
  24. Suenaga H, Koyama Y, Miyakoshi M, Miyazaki R, Yano H, Sota M, et al. 2009. Novel organization of aromatic degradation pathway genes in a microbial community as revealed by metagenomic analysis. ISME J. 3: 1335-1348. https://doi.org/10.1038/ismej.2009.76
  25. Yang M, Jarrett SG, Graven R, Kaetzel DM. 2009. YNK1, the yeast homolog of human metastasis suppressor NM23, is required for repair of UV radiation- and etopside-induced DNA damage. Mutat. Res. 660: 74-78. https://doi.org/10.1016/j.mrfmmm.2008.09.015

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